TRB2_ARATH
ID TRB2_ARATH Reviewed; 299 AA.
AC Q9FJW5; Q8VX38;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Telomere repeat-binding factor 2;
DE Short=AtTRB2;
DE AltName: Full=MYB transcription factor;
DE AltName: Full=Telomere-binding protein 3;
DE Short=AtTBP3;
GN Name=TRB2; Synonyms=TBP3; OrderedLocusNames=At5g67580; ORFNames=K9I9.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RA Sprenger M., Weisshaar B.;
RT "Identification and functional characterisation of the Arabidopsis telomere
RT repeat binding factor TRB2.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Qu L.-J., Gu H.;
RT "The MYB transcription factor family in Arabidopsis: a genome-wide cloning
RT and expression pattern analysis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP GENE FAMILY.
RX PubMed=14576282; DOI=10.1104/pp.103.026856;
RA Marian C.O., Bordoli S.J., Goltz M., Santarella R.A., Jackson L.P.,
RA Danilevskaya O., Beckstette M., Meeley R., Bass H.W.;
RT "The maize Single myb histone 1 gene, Smh1, belongs to a novel gene family
RT and encodes a protein that binds telomere DNA repeats in vitro.";
RL Plant Physiol. 133:1336-1350(2003).
RN [7]
RP HOMOMULTIMERIZATION, AND INTERACTION WITH TRB1 AND TRB3.
RX PubMed=15589838; DOI=10.1016/j.febslet.2004.11.021;
RA Kuchar M., Fajkus J.;
RT "Interactions of putative telomere-binding proteins in Arabidopsis
RT thaliana: identification of functional TRF2 homolog in plants.";
RL FEBS Lett. 578:311-315(2004).
RN [8]
RP TISSUE SPECIFICITY, HOMODIMERIZATION, INTERACTION WITH TRB3, AND
RP DNA-BINDING.
RX PubMed=15060584; DOI=10.1139/g03-136;
RA Schrumpfova P., Kuchar M., Mikova G., Skrisovska L., Kubicarova T.,
RA Fajkus J.;
RT "Characterization of two Arabidopsis thaliana myb-like proteins showing
RT affinity to telomeric DNA sequence.";
RL Genome 47:316-324(2004).
RN [9]
RP GENE FAMILY.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [10]
RP INTERACTION WITH TRB1.
RX PubMed=18387366; DOI=10.1016/j.febslet.2008.03.034;
RA Schrumpfova P.P., Kuchar M., Palecek J., Fajkus J.;
RT "Mapping of interaction domains of putative telomere-binding proteins
RT AtTRB1 and AtPOT1b from Arabidopsis thaliana.";
RL FEBS Lett. 582:1400-1406(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19947985; DOI=10.1111/j.1365-313x.2009.04094.x;
RA Dvorackova M., Rossignol P., Shaw P.J., Koroleva O.A., Doonan J.H.,
RA Fajkus J.;
RT "AtTRB1, a telomeric DNA-binding protein from Arabidopsis, is concentrated
RT in the nucleolus and shows highly dynamic association with chromatin.";
RL Plant J. 61:637-649(2010).
CC -!- FUNCTION: Binds preferentially double-stranded telomeric repeats, but
CC it can also bind to the single G-rich telomeric strand.
CC -!- SUBUNIT: Forms a homodimer and heterodimers with TRB1 or TRB3.
CC Interacts with TRB1 and TRB3. {ECO:0000269|PubMed:15060584,
CC ECO:0000269|PubMed:15589838, ECO:0000269|PubMed:18387366}.
CC -!- INTERACTION:
CC Q9FJW5; Q8VWK4: TRB1; NbExp=4; IntAct=EBI-476115, EBI-476101;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:19947985}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:19947985}. Chromosome
CC {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:19947985}.
CC Note=Localized to the nucleolus during interphase.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15060584}.
CC -!- DOMAIN: HTH myb-type domain confers double-stranded telomeric DNA-
CC binding while the H15 domain is involved in non-specific DNA-protein
CC interaction and multimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. SMH subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00837}.
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DR EMBL; U83836; AAL73442.1; -; Genomic_DNA.
DR EMBL; U83837; AAL73441.1; -; mRNA.
DR EMBL; AY519545; AAS10015.1; -; mRNA.
DR EMBL; AB013390; BAB08466.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98362.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98363.1; -; Genomic_DNA.
DR EMBL; AY039883; AAK63987.1; -; mRNA.
DR EMBL; AY077668; AAL76146.1; -; mRNA.
DR RefSeq; NP_201559.1; NM_126158.3.
DR RefSeq; NP_851286.1; NM_180955.3.
DR AlphaFoldDB; Q9FJW5; -.
DR BMRB; Q9FJW5; -.
DR SMR; Q9FJW5; -.
DR BioGRID; 22136; 15.
DR IntAct; Q9FJW5; 13.
DR MINT; Q9FJW5; -.
DR STRING; 3702.AT5G67580.1; -.
DR iPTMnet; Q9FJW5; -.
DR PaxDb; Q9FJW5; -.
DR PRIDE; Q9FJW5; -.
DR ProteomicsDB; 228388; -.
DR EnsemblPlants; AT5G67580.1; AT5G67580.1; AT5G67580.
DR EnsemblPlants; AT5G67580.2; AT5G67580.2; AT5G67580.
DR GeneID; 836894; -.
DR Gramene; AT5G67580.1; AT5G67580.1; AT5G67580.
DR Gramene; AT5G67580.2; AT5G67580.2; AT5G67580.
DR KEGG; ath:AT5G67580; -.
DR Araport; AT5G67580; -.
DR TAIR; locus:2158611; AT5G67580.
DR eggNOG; ENOG502QSU2; Eukaryota.
DR HOGENOM; CLU_047477_0_1_1; -.
DR InParanoid; Q9FJW5; -.
DR OMA; DMKLAHG; -.
DR OrthoDB; 1114012at2759; -.
DR PhylomeDB; Q9FJW5; -.
DR PRO; PR:Q9FJW5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJW5; baseline and differential.
DR Genevisible; Q9FJW5; AT.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:TAIR.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR044597; SMH1-6.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46267; PTHR46267; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..299
FT /note="Telomere repeat-binding factor 2"
FT /id="PRO_0000417011"
FT DOMAIN 1..61
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 121..189
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DNA_BIND 28..57
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 93..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..288
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="T -> S (in Ref. 1; AAL73441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 33014 MW; C9F767444914A409 CRC64;
MGAPKQKWTP EEEAALKAGV LKHGTGKWRT ILSDTEFSLI LKSRSNVDLK DKWRNISVTA
LWGSRKKAKL ALKRTPPGTK QDDNNTALTI VALTNDDERA KPTSPGGSGG GSPRTCASKR
SITSLDKIIF EAITNLRELR GSDRTSIFLY IEENFKTPPN MKRHVAVRLK HLSSNGTLVK
IKHKYRFSSN FIPAGARQKA PQLFLEGNNK KDPTKPEENG ANSLTKFRVD GELYMIKGMT
AQEAAEAAAR AVAEAEFAIT EAEQAAKEAE RAEAEAEAAQ IFAKAAMKAL KFRIRNHPW
